The polymer radius of gyration (\(R_g\) ) or end-to-end distance (\(R_{ee}\) ) are common measurable properties of the polymer's ensemble average structure. However, the Flory exponent is a more convenient parameter to compare between structural compactness of polymers with a different number of residues (\(N\) ) as \(R_g \propto R_{ee} \propto N^{\nu }\)  [1]}. For example, this was used to show that denatured unfolded protein behave as excluded volume random coils with \(\nu =0.598 \pm 0.028\)  [2]}. On average across different sequences, IDPs behave as ideal chain (or chain in \(\theta \) -solvent) with \(\nu =0.522 \pm 0.01\)  [3]}. The latter indicated that IDPs are more compact than chemically denatured proteins and that individual IDPs can show large deviations from the average value. Hofmann et al. have shown that the unfolded state of a globular protein can be modeled using polymer-like statistics with \(\nu =0.46 \pm 0.05\)  and that IDPs are more expanded [4]}. Recently, using molecular dynamics (MD) simulation, it was shown that IDPs scale as \(\nu =0.53 \pm 0.03\)  [5]} opposed to another MD simulation that showed scaling behaviour \(\nu \approx 0.588\)  [6]}.
